3POS

Crystal structure of the globular domain of human calreticulin

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005509	molecular_function	calcium ion binding
A	0005783	cellular_component	endoplasmic reticulum
A	0006457	biological_process	protein folding
A	0051082	molecular_function	unfolded protein binding
B	0005509	molecular_function	calcium ion binding
B	0005783	cellular_component	endoplasmic reticulum
B	0006457	biological_process	protein folding
B	0051082	molecular_function	unfolded protein binding
C	0005509	molecular_function	calcium ion binding
C	0005783	cellular_component	endoplasmic reticulum
C	0006457	biological_process	protein folding
C	0051082	molecular_function	unfolded protein binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA A 1

Chain	Residue
A	GLN26
A	LYS62
A	LYS64
A	ASP328
A	HOH728
A	HOH730

---

site_id	AC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA B 2

Chain	Residue
B	ASP328
B	HOH725
B	HOH726
B	GLN26
B	LYS62
B	LYS64

---

site_id	AC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA C 3

Chain	Residue
C	GLN26
C	LYS62
C	LYS64
C	ASP328
C	HOH727
C	HOH729

---

Functional Information from PROSITE/UniProt

site_id	PS00803
Number of Residues	16
Details	CALRETICULIN_1 Calreticulin family signature 1. KhEQnidCGGGYVKLF

Chain	Residue	Details
A	LYS98-PHE113

---

site_id	PS00804
Number of Residues	9
Details	CALRETICULIN_2 Calreticulin family signature 2. IMFGPDiCG

Chain	Residue	Details
A	ILE130-GLY138

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	12
Details	BINDING: BINDING => ECO:0000269|PubMed:21423620, ECO:0000269|PubMed:27840680, ECO:0007744|PDB:3POS, ECO:0007744|PDB:3POW, ECO:0007744|PDB:5LK5

Chain	Residue	Details
A	GLN26
C	LYS62
C	LYS64
C	ASP328
A	LYS62
A	LYS64
A	ASP328
B	GLN26
B	LYS62
B	LYS64
B	ASP328
C	GLN26

---

site_id	SWS_FT_FI2
Number of Residues	15
Details	BINDING: BINDING => ECO:0000250|UniProtKB:P14211

Chain	Residue	Details
A	TYR109
B	ASP317
C	TYR109
C	LYS111
C	TYR128
C	ASP135
C	ASP317
A	LYS111
A	TYR128
A	ASP135
A	ASP317
B	TYR109
B	LYS111
B	TYR128
B	ASP135

---

site_id	SWS_FT_FI3
Number of Residues	6
Details	MOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861

Chain	Residue	Details
A	LYS48
A	LYS159
B	LYS48
B	LYS159
C	LYS48
C	LYS159

---

site_id	SWS_FT_FI4
Number of Residues	3
Details	MOD_RES: N6-(2-hydroxyisobutyryl)lysine => ECO:0000269|PubMed:29192674

Chain	Residue	Details
A	LYS64
B	LYS64
C	LYS64

---

site_id	SWS_FT_FI5
Number of Residues	3
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19159218

Chain	Residue	Details
A	ASN344
B	ASN344
C	ASN344

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